1fns

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(New page: 200px<br /> <applet load="1fns" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fns, resolution 2.00&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1fns.gif|left|200px]]<br />
 
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<applet load="1fns" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fns, resolution 2.00&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR (VWF) A1 DOMAIN I546V MUTANT IN COMPLEX WITH THE FUNCTION BLOCKING FAB NMC4'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR (VWF) A1 DOMAIN I546V MUTANT IN COMPLEX WITH THE FUNCTION BLOCKING FAB NMC4==
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Platelet participation in hemostasis and arterial thrombosis requires the, binding of glycoprotein (GP) Ibalpha to von Willebrand factor (vWF)., Hemodynamic forces enhance this interaction, an effect mimicked by the, substitution I546V in the vWF A1 domain. A water molecule becomes, internalized near the deleted Ile methyl group. The change in, hydrophobicity of the local environment causes positional changes, propagated over a distance of 27 A. As a consequence, a major, reorientation of a peptide plane occurs in a surface loop involved in GP, Ibalpha binding. This distinct vWF conformation shows increased platelet, adhesion and provides a structural model for the initial regulation of, thrombus formation.
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<StructureSection load='1fns' size='340' side='right'caption='[[1fns]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fns]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FNS FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fns OCA], [https://pdbe.org/1fns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fns RCSB], [https://www.ebi.ac.uk/pdbsum/1fns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fns ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IGKC_MOUSE IGKC_MOUSE]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fn/1fns_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fns ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Platelet participation in hemostasis and arterial thrombosis requires the binding of glycoprotein (GP) Ibalpha to von Willebrand factor (vWF). Hemodynamic forces enhance this interaction, an effect mimicked by the substitution I546V in the vWF A1 domain. A water molecule becomes internalized near the deleted Ile methyl group. The change in hydrophobicity of the local environment causes positional changes propagated over a distance of 27 A. As a consequence, a major reorientation of a peptide plane occurs in a surface loop involved in GP Ibalpha binding. This distinct vWF conformation shows increased platelet adhesion and provides a structural model for the initial regulation of thrombus formation.
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==Disease==
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von Willebrand factor conformation and adhesive function is modulated by an internalized water molecule.,Celikel R, Ruggeri ZM, Varughese KI Nat Struct Biol. 2000 Oct;7(10):881-4. PMID:11017197<ref>PMID:11017197</ref>
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Known diseases associated with this structure: von Willebrand disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=193400 193400]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1FNS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FNS OCA].
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</div>
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<div class="pdbe-citations 1fns" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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von Willebrand factor conformation and adhesive function is modulated by an internalized water molecule., Celikel R, Ruggeri ZM, Varughese KI, Nat Struct Biol. 2000 Oct;7(10):881-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11017197 11017197]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Varughese KI]]
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[[Category: Varughese, K.I.]]
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[[Category: blood coagulation type 2b von willebrand disease]]
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[[Category: complex (willebrand/immunoglobulin)]]
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[[Category: glycoprotein iba (a:alpha) binding]]
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[[Category: von willebrand factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:55:33 2007''
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Current revision

CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR (VWF) A1 DOMAIN I546V MUTANT IN COMPLEX WITH THE FUNCTION BLOCKING FAB NMC4

PDB ID 1fns

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